Defective proximal tubule lysosomal acidification by Bence Jones proteins: An immunoelectron microscopy study
Proximal tubule handling of two human Bence Jones proteins (neutral and acidic BJP) was evaluated using protein A-gold labelling. After 30 min of acute light-chain infusion into 6 rats (alone or in combination with dinitrophenyl-aminopropyl-methylamine [DAMP]), kidney biopsies were processed for imm...
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| Veröffentlicht in: | Experimental nephrology 1998-11, Vol.6 (6), p.514-521 |
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| creator | NICASTRI, A. L BRANDAO DE ALMEIDA PRADO, M. J SESSO, A BRANDAO DE ALMEIDA PRADO, E |
| description | Proximal tubule handling of two human Bence Jones proteins (neutral and acidic BJP) was evaluated using protein A-gold labelling. After 30 min of acute light-chain infusion into 6 rats (alone or in combination with dinitrophenyl-aminopropyl-methylamine [DAMP]), kidney biopsies were processed for immunoelectron microscopy. Antibodies directed at monoclonal lambda light chains, mannose-6-phosphate cation-independent receptor (MPR) and DAMP were used. Labelling density (number of pA-gold particles/micrometer2), expressed as median (25-75 percentiles), differed (p < 0.05) between the two BJP, being 94.5 (32.9-212.5) vs. 19.4 (3.7-45.6) pA-gold/ micrometer2++ in endocytic vacuoles, and 297.3 (207.1-382.1) vs. 83.2 (16. 6-197.0) pA-gold/ micrometer2 in non-vacuolar electrondense endosome-lysosome structures. Labelling density for MPR was 47.7 (22. 2-84.6) vs. 4.0 (2.7-6.3) pA-gold/micrometer2. The area of MPR-labelled structures was also different, i.e.: 0.2 (0.1-0.4) vs. 0.9 (0.5-1.8) micrometer2. The endosome-lysosome pH distribution range differed significantly: 6.8 (6.4-7.0) vs. 6.3 (5.8-7.0). There was a significant accumulation of neutral BJP in endocytic structures, an acidification deficit of pre-lysosomes/lysosomes and MPR retention, suggestive of defective receptor recycling with this BJP. Interference with the physiological process of lysosomal acidification may be an important mechanism of higher nephrotoxicity in some BJP. |
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L ; BRANDAO DE ALMEIDA PRADO, M. J ; SESSO, A ; BRANDAO DE ALMEIDA PRADO, E</creator><creatorcontrib>NICASTRI, A. L ; BRANDAO DE ALMEIDA PRADO, M. J ; SESSO, A ; BRANDAO DE ALMEIDA PRADO, E</creatorcontrib><description>Proximal tubule handling of two human Bence Jones proteins (neutral and acidic BJP) was evaluated using protein A-gold labelling. After 30 min of acute light-chain infusion into 6 rats (alone or in combination with dinitrophenyl-aminopropyl-methylamine [DAMP]), kidney biopsies were processed for immunoelectron microscopy. Antibodies directed at monoclonal lambda light chains, mannose-6-phosphate cation-independent receptor (MPR) and DAMP were used. Labelling density (number of pA-gold particles/micrometer2), expressed as median (25-75 percentiles), differed (p < 0.05) between the two BJP, being 94.5 (32.9-212.5) vs. 19.4 (3.7-45.6) pA-gold/ micrometer2++ in endocytic vacuoles, and 297.3 (207.1-382.1) vs. 83.2 (16. 6-197.0) pA-gold/ micrometer2 in non-vacuolar electrondense endosome-lysosome structures. Labelling density for MPR was 47.7 (22. 2-84.6) vs. 4.0 (2.7-6.3) pA-gold/micrometer2. The area of MPR-labelled structures was also different, i.e.: 0.2 (0.1-0.4) vs. 0.9 (0.5-1.8) micrometer2. The endosome-lysosome pH distribution range differed significantly: 6.8 (6.4-7.0) vs. 6.3 (5.8-7.0). There was a significant accumulation of neutral BJP in endocytic structures, an acidification deficit of pre-lysosomes/lysosomes and MPR retention, suggestive of defective receptor recycling with this BJP. Interference with the physiological process of lysosomal acidification may be an important mechanism of higher nephrotoxicity in some BJP.</description><identifier>ISSN: 1018-7782</identifier><identifier>PMID: 9807023</identifier><language>eng</language><publisher>Basel: Karger</publisher><subject>Acids - metabolism ; Animals ; Bence Jones Protein - chemistry ; Bence Jones Protein - metabolism ; Biological and medical sciences ; Blotting, Western ; Dinitrobenzenes - pharmacokinetics ; Electrophoresis, Polyacrylamide Gel ; Hematologic and hematopoietic diseases ; Humans ; Hydrogen-Ion Concentration ; Kidney Tubules, Proximal - metabolism ; Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis ; Lysosomes - metabolism ; Male ; Medical sciences ; Microscopy, Immunoelectron ; Rats ; Rats, Wistar ; Receptor, IGF Type 2 - metabolism</subject><ispartof>Experimental nephrology, 1998-11, Vol.6 (6), p.514-521</ispartof><rights>1999 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1593468$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9807023$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>NICASTRI, A. L</creatorcontrib><creatorcontrib>BRANDAO DE ALMEIDA PRADO, M. J</creatorcontrib><creatorcontrib>SESSO, A</creatorcontrib><creatorcontrib>BRANDAO DE ALMEIDA PRADO, E</creatorcontrib><title>Defective proximal tubule lysosomal acidification by Bence Jones proteins: An immunoelectron microscopy study</title><title>Experimental nephrology</title><addtitle>Exp Nephrol</addtitle><description>Proximal tubule handling of two human Bence Jones proteins (neutral and acidic BJP) was evaluated using protein A-gold labelling. After 30 min of acute light-chain infusion into 6 rats (alone or in combination with dinitrophenyl-aminopropyl-methylamine [DAMP]), kidney biopsies were processed for immunoelectron microscopy. Antibodies directed at monoclonal lambda light chains, mannose-6-phosphate cation-independent receptor (MPR) and DAMP were used. Labelling density (number of pA-gold particles/micrometer2), expressed as median (25-75 percentiles), differed (p < 0.05) between the two BJP, being 94.5 (32.9-212.5) vs. 19.4 (3.7-45.6) pA-gold/ micrometer2++ in endocytic vacuoles, and 297.3 (207.1-382.1) vs. 83.2 (16. 6-197.0) pA-gold/ micrometer2 in non-vacuolar electrondense endosome-lysosome structures. Labelling density for MPR was 47.7 (22. 2-84.6) vs. 4.0 (2.7-6.3) pA-gold/micrometer2. The area of MPR-labelled structures was also different, i.e.: 0.2 (0.1-0.4) vs. 0.9 (0.5-1.8) micrometer2. The endosome-lysosome pH distribution range differed significantly: 6.8 (6.4-7.0) vs. 6.3 (5.8-7.0). There was a significant accumulation of neutral BJP in endocytic structures, an acidification deficit of pre-lysosomes/lysosomes and MPR retention, suggestive of defective receptor recycling with this BJP. Interference with the physiological process of lysosomal acidification may be an important mechanism of higher nephrotoxicity in some BJP.</description><subject>Acids - metabolism</subject><subject>Animals</subject><subject>Bence Jones Protein - chemistry</subject><subject>Bence Jones Protein - metabolism</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Dinitrobenzenes - pharmacokinetics</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Hematologic and hematopoietic diseases</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kidney Tubules, Proximal - metabolism</subject><subject>Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis</subject><subject>Lysosomes - metabolism</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Microscopy, Immunoelectron</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Receptor, IGF Type 2 - metabolism</subject><issn>1018-7782</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9j0tLxDAUhbNQxnH0JwhZuC00TTpJ3Y3jmwE3uh7yuIFIk5QmFfvvzWBxdS7nO_fAOUNrUhNRcS6aC3SZ0ldd17zm7QqtOlGuhq6RfwALOrtvwMMYf5yXPc6TmnrA_ZxiiidDamecdVpmFwNWM76HoAG_xQDp9JbBhXSHdwE776cQoS-VY4l6p8eYdBxmnPJk5it0bmWf4HrRDfp8evzYv1SH9-fX_e5QDQ1tcwVCGcU7YZnQLVhJDVOG0YYToTuqgRCjuq1l20IJp7xjDJQkEgQ0DbOGbtDNX-8wKQ_mOIxl2Dgfl9mF3y5cJi17O8qgXfqPkbajbCvoL-iQYwU</recordid><startdate>19981101</startdate><enddate>19981101</enddate><creator>NICASTRI, A. L</creator><creator>BRANDAO DE ALMEIDA PRADO, M. J</creator><creator>SESSO, A</creator><creator>BRANDAO DE ALMEIDA PRADO, E</creator><general>Karger</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>19981101</creationdate><title>Defective proximal tubule lysosomal acidification by Bence Jones proteins: An immunoelectron microscopy study</title><author>NICASTRI, A. L ; BRANDAO DE ALMEIDA PRADO, M. J ; SESSO, A ; BRANDAO DE ALMEIDA PRADO, E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p235t-e8bdb798f48c5efa3d4bd432718c93ce11db96f46c5e1737944eba1ae8e224fd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Acids - metabolism</topic><topic>Animals</topic><topic>Bence Jones Protein - chemistry</topic><topic>Bence Jones Protein - metabolism</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Dinitrobenzenes - pharmacokinetics</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Hematologic and hematopoietic diseases</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kidney Tubules, Proximal - metabolism</topic><topic>Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis</topic><topic>Lysosomes - metabolism</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Microscopy, Immunoelectron</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Receptor, IGF Type 2 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>NICASTRI, A. L</creatorcontrib><creatorcontrib>BRANDAO DE ALMEIDA PRADO, M. J</creatorcontrib><creatorcontrib>SESSO, A</creatorcontrib><creatorcontrib>BRANDAO DE ALMEIDA PRADO, E</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>Experimental nephrology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>NICASTRI, A. L</au><au>BRANDAO DE ALMEIDA PRADO, M. J</au><au>SESSO, A</au><au>BRANDAO DE ALMEIDA PRADO, E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Defective proximal tubule lysosomal acidification by Bence Jones proteins: An immunoelectron microscopy study</atitle><jtitle>Experimental nephrology</jtitle><addtitle>Exp Nephrol</addtitle><date>1998-11-01</date><risdate>1998</risdate><volume>6</volume><issue>6</issue><spage>514</spage><epage>521</epage><pages>514-521</pages><issn>1018-7782</issn><abstract>Proximal tubule handling of two human Bence Jones proteins (neutral and acidic BJP) was evaluated using protein A-gold labelling. After 30 min of acute light-chain infusion into 6 rats (alone or in combination with dinitrophenyl-aminopropyl-methylamine [DAMP]), kidney biopsies were processed for immunoelectron microscopy. Antibodies directed at monoclonal lambda light chains, mannose-6-phosphate cation-independent receptor (MPR) and DAMP were used. Labelling density (number of pA-gold particles/micrometer2), expressed as median (25-75 percentiles), differed (p < 0.05) between the two BJP, being 94.5 (32.9-212.5) vs. 19.4 (3.7-45.6) pA-gold/ micrometer2++ in endocytic vacuoles, and 297.3 (207.1-382.1) vs. 83.2 (16. 6-197.0) pA-gold/ micrometer2 in non-vacuolar electrondense endosome-lysosome structures. Labelling density for MPR was 47.7 (22. 2-84.6) vs. 4.0 (2.7-6.3) pA-gold/micrometer2. The area of MPR-labelled structures was also different, i.e.: 0.2 (0.1-0.4) vs. 0.9 (0.5-1.8) micrometer2. The endosome-lysosome pH distribution range differed significantly: 6.8 (6.4-7.0) vs. 6.3 (5.8-7.0). There was a significant accumulation of neutral BJP in endocytic structures, an acidification deficit of pre-lysosomes/lysosomes and MPR retention, suggestive of defective receptor recycling with this BJP. Interference with the physiological process of lysosomal acidification may be an important mechanism of higher nephrotoxicity in some BJP.</abstract><cop>Basel</cop><pub>Karger</pub><pmid>9807023</pmid><tpages>8</tpages></addata></record> |
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| subjects | Acids - metabolism Animals Bence Jones Protein - chemistry Bence Jones Protein - metabolism Biological and medical sciences Blotting, Western Dinitrobenzenes - pharmacokinetics Electrophoresis, Polyacrylamide Gel Hematologic and hematopoietic diseases Humans Hydrogen-Ion Concentration Kidney Tubules, Proximal - metabolism Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis Lysosomes - metabolism Male Medical sciences Microscopy, Immunoelectron Rats Rats, Wistar Receptor, IGF Type 2 - metabolism |
| title | Defective proximal tubule lysosomal acidification by Bence Jones proteins: An immunoelectron microscopy study |
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